Heterogeneous nucleation of hydroxyapatite on protein: structural effect of silk sericin

Acidic proteins play an important role during mineral formation in biological systems, but the mechanism of mineral formation is far from understood. In this paper, we report on the relationship between the structure of a protein and hydroxyapatite deposition under biomimetic conditions. Sericin, a...

Full description

Saved in:
Bibliographic Details
Published in:Journal of the Royal Society interface Vol. 2; no. 4; pp. 373 - 378
Main Authors: Takeuchi, Akari, Ohtsuki, Chikara, Miyazaki, Toshiki, Kamitakahara, Masanobu, Ogata, Shin-ichi, Yamazaki, Masao, Furutani, Yoshiaki, Kinoshita, Hisao, Tanihara, Masao
Format: Journal Article
Language:English
Published: London The Royal Society 22-09-2005
Subjects:
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:Acidic proteins play an important role during mineral formation in biological systems, but the mechanism of mineral formation is far from understood. In this paper, we report on the relationship between the structure of a protein and hydroxyapatite deposition under biomimetic conditions. Sericin, a type of silk protein, was adopted as a suitable protein for studying structural effect on hydroxyapatite deposition, since it forms a hydroxyapatite layer on its surface in a metastable calcium phosphate solution, and its structure has been reported. Sericin effectively induced hydroxyapatite nucleation when it has high molecular weight and a β sheet structure. This indicates that the specific structure of a protein can effectively induce heterogeneous nucleation of hydroxyapatite in a biomimetic solution, i.e. a metastable calcium phosphate solution. This finding is useful in understanding biomineralization, as well as for the design of organic polymers that can effectively induce hydroxyapatite nucleation.
Bibliography:istex:C005116DA54001FFD9BB8D4CD1F483F294BC9996
ArticleID:rsif20050052
Author for correspondence
ark:/67375/V84-R1T9MTDM-W
href:373.pdf
ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-1
content type line 23
ObjectType-Article-1
ObjectType-Feature-2
ISSN:1742-5689
1742-5662
DOI:10.1098/rsif.2005.0052